Evidence map›Paper›PMID 12149480›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase.

Christopher S Brower, Shigeo Sato, Chieri Tomomori-Sato, Takumi Kamura, Arnim Pause, Robert Stearman, Richard D Klausner, Sohail Malik, William S Lane, Irina Sorokina and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

40 citing papers in PubMed, 82 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Disordered proteinaceous machines.Chemical reviews · 2014
    Review
  9. Article
  10. Article
  11. Article
  12. Ubiquitin and proteasomes in transcription.Annual review of biochemistry · 2012
    Review
  13. Article
  14. Article
  15. Mediator and human disease.Seminars in cell & developmental biology · 2011
    Review
  16. Origins and activity of the Mediator complex.Seminars in cell & developmental biology · 2011
    Review
  17. Article
  18. Article
  19. Szt2, a novel gene for seizure threshold in mice.Genes, brain, and behavior · 2009
    Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors at 4 institutions in 1 country.

Christopher S BrowerStowers Institute for Medical Research, Kansas City, MO 64110, USA.
Shigeo Sato
Chieri Tomomori-Sato
Takumi Kamura
Arnim Pause
Robert Stearman
Richard D Klausner
Sohail Malik
William S Lane
Irina Sorokina
Robert G Roeder
Joan Weliky Conaway
Ronald C Conaway
Harvard University · USRockefeller University · USStowers Institute for Medical Research · USUniversity of Kansas Medical Center · US

Funding

BIOCHEMISTRY OF EUKARYOTIC MESSENGER RNA SYNTHESISR37GM041628 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI CONAWAY, RONALD C. · 2000 to 2009
$3.8M
NIGMS NIH HHS R37 GM041628NIGMS NIH HHS R37 GM41628
6 · The paper itself

Abstract

The heterodimeric Elongin BC complex has been shown to interact in vitro and in cells with a conserved BC-box motif found in an increasing number of proteins including RNA polymerase II elongation factor Elongin A, suppressor of cytokine signaling (SOCS)-box proteins, and the von Hippel-Lindau tumor suppressor protein. Recently, the Elongin BC complex was found to function as an adaptor that links these BC-box proteins to a module composed of Cullin family members Cul2 or Cul5 and RING-H2 finger protein Rbx1 to reconstitute a family of E3 ubiquitin ligases that activate ubiquitylation by the E2 ubiquitin-conjugating enzyme Ubc5. As part of our effort to understand the functions of Elongin BC-based ubiquitin ligases, we exploited a modified yeast two-hybrid screen to identify a mammalian BC-box protein similar in sequence to Saccharomyces cerevisiae Mediator subunit Med8p. In this report we demonstrate (i) that mammalian MED8 is a subunit of the mammalian Mediator complex and (ii) that MED8 can assemble with Elongins B and C, Cul2, and Rbx1 to reconstitute a ubiquitin ligase. Taken together, our findings are consistent with the model that MED8 could function to recruit ubiquitin ligase activity directly to the RNA polymerase II transcriptional machinery.

Indexed as

Cullin ProteinsSaccharomyces cerevisiae ProteinsUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesAmino Acid SequenceAnimalsBase SequenceBinding SitesCell Cycle ProteinsCell LineCell Line, TransformedDimerizationDNA, ComplementaryElonginFungal ProteinsHumansCell Cycle ProteinsCUL2 protein, humanCullin ProteinsDNA, ComplementaryELOA protein, humanEloa protein, mouseEloa protein, ratElonginFungal ProteinsLigasesMED8 protein, ratMediator ComplexNuclear ProteinsNUT2 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsTranscription FactorsTumor Suppressor ProteinsUBC5 protein, S cerevisiaeUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesVHL protein, humanVon Hippel-Lindau Tumor Suppressor Protein

Identifiers

PMID12149480
PMCPMC124918
OpenAlexW2166793463

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.